HHP2_ARATH
ID HHP2_ARATH Reviewed; 358 AA.
AC Q84N34; O65564; Q8VXZ4;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Heptahelical transmembrane protein 2;
DE AltName: Full=PAQR family protein HHP2;
GN Name=HHP2; OrderedLocusNames=At4g30850; ORFNames=F6I18.240;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY,
RP AND INDUCTION.
RX PubMed=16263907; DOI=10.1093/jxb/eri311;
RA Hsieh M.H., Goodman H.M.;
RT "A novel gene family in Arabidopsis encoding putative heptahelical
RT transmembrane proteins homologous to human adiponectin receptors and
RT progestin receptors.";
RL J. Exp. Bot. 56:3137-3147(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in abiotic stress response. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and at lower levels in
CC stems and flowers. {ECO:0000269|PubMed:16263907}.
CC -!- INDUCTION: By abscisic acid (ABA) and the cytokinin benzyladenine (BA).
CC {ECO:0000269|PubMed:16263907}.
CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA18208.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79803.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY267331; AAP23168.1; -; mRNA.
DR EMBL; AL022198; CAA18208.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161577; CAB79803.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85819.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85820.1; -; Genomic_DNA.
DR EMBL; AY074328; AAL67024.1; -; mRNA.
DR EMBL; BT021124; AAX22259.1; -; mRNA.
DR EMBL; BT025258; ABF19011.1; -; mRNA.
DR PIR; B85361; B85361.
DR RefSeq; NP_194814.2; NM_119232.3.
DR RefSeq; NP_974643.1; NM_202914.1.
DR AlphaFoldDB; Q84N34; -.
DR SMR; Q84N34; -.
DR BioGRID; 14496; 335.
DR IntAct; Q84N34; 337.
DR STRING; 3702.AT4G30850.2; -.
DR PaxDb; Q84N34; -.
DR PRIDE; Q84N34; -.
DR ProteomicsDB; 230203; -.
DR EnsemblPlants; AT4G30850.1; AT4G30850.1; AT4G30850.
DR EnsemblPlants; AT4G30850.2; AT4G30850.2; AT4G30850.
DR GeneID; 829209; -.
DR Gramene; AT4G30850.1; AT4G30850.1; AT4G30850.
DR Gramene; AT4G30850.2; AT4G30850.2; AT4G30850.
DR KEGG; ath:AT4G30850; -.
DR Araport; AT4G30850; -.
DR TAIR; locus:2126709; AT4G30850.
DR eggNOG; KOG0748; Eukaryota.
DR HOGENOM; CLU_023075_4_0_1; -.
DR InParanoid; Q84N34; -.
DR OMA; CLESIFW; -.
DR OrthoDB; 1524940at2759; -.
DR PhylomeDB; Q84N34; -.
DR PRO; PR:Q84N34; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84N34; baseline and differential.
DR Genevisible; Q84N34; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0009725; P:response to hormone; IEP:TAIR.
DR GO; GO:0009744; P:response to sucrose; IEP:TAIR.
DR InterPro; IPR004254; AdipoR/HlyIII-related.
DR PANTHER; PTHR20855; PTHR20855; 1.
DR Pfam; PF03006; HlyIII; 1.
PE 2: Evidence at transcript level;
KW Membrane; Reference proteome; Stress response; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..358
FT /note="Heptahelical transmembrane protein 2"
FT /id="PRO_0000430048"
FT TOPO_DOM 1..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 246..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 278..283
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 119
FT /note="M -> I (in Ref. 4; AAL67024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 358 AA; 41025 MW; 9F57E7AD57D3AFC1 CRC64;
MQKRRTVKES TKIRNGKGMD SGEKKRSEKR LMKFEELPRY LKDNEFIHNH YRCEWSIKET
FLSAFSWHNE TLNIWTHLCG FAIFTWMMVV SSMETTELGL AGFVSLLSGA TIRWPWPSMA
MSKDVYFSSD QTLHHDLNVT HTRSLLNSQG DVNYEAIPKW PWLVFLTGAM GCLICSSMSH
LFACHSRRFN LFFWRLDYAG ISLMIVCSFF APIYYAFSCH TYWRLFYLSS ISILGLLAIF
TLLSPSLSAP RFRSFRAALF LTMGFSGVIP ATHVLYLHKD HPNVLIALVY ELAMAVLYAT
GAAFYVTRIP ERWKPGAFDI AGHSHQIFHV FVVLGALAHS VASLLIMDFR RASPSCAF
